The activity of soluble protein kinase (ATP: protein phosphotransferase) and pattern of nuclear protein phosphorylation was monitored in cultured rat pineal glands during the induction of serotonin N acetyltransferase (acetyl CoA:serotonin N acetyltransferase) by l isoproterenol. A nuclear protein appears to be phosphorylated during the early stages of enzyme induction but is not phosphorylated at later stages of induction. This correlates well with the need for RNA synthesis associated with the induction process. The nuclear protein was also phosphorylated when the pineal glands were treated with dibutyryl 3':5' cyclic AMP. The soluble protein kinase activity appeared to decline during mid to late stages of enzyme induction, but there was no concomitant increase in the particulate protein kinase activity.
|Number of pages||4|
|Journal||Proceedings of the National Academy of Sciences of the United States of America|
|State||Published - Jan 1 1977|